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Actin Polymerization and Cell Motility

Actin Polymerization and Cell Motility

Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.

Actin Filament Depolymerization

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

Introduction to Actin

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across different species.

Cytoskeletal Accessory Proteins

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...

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Related Experiment Video

Updated: Jun 17, 2026

Investigating the Function of Coronin A in the Early Starvation Response of Dictyostelium discoideum by Aggregation Assays

Investigating the Function of Coronin A in the Early Starvation Response of Dictyostelium discoideum by Aggregation Assays

Published on: June 18, 2016

A Coronin7 homolog with functions in actin-driven processes.

Maria C Shina¹, Can Unal, Ludwig Eichinger

¹Institute for Biochemistry I, Center for Molecular Medicine Cologne and Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases, Medical Faculty, University of Cologne, 50931 Koeln, Germany.

The Journal of Biological Chemistry

|January 15, 2010

Summary

Dictyostelium discoideum Coronin7 (DdCRN7) binds F-actin, protecting it from depolymerization. This interaction is key to its role in cell movement and phagocytosis.

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MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a

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Related Experiment Videos

Last Updated: Jun 17, 2026

Investigating the Function of Coronin A in the Early Starvation Response of Dictyostelium discoideum by Aggregation Assays

Investigating the Function of Coronin A in the Early Starvation Response of Dictyostelium discoideum by Aggregation Assays

Published on: June 18, 2016

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a

MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a

Published on: August 23, 2024

Area of Science:

Cell Biology
Cytoskeletal Dynamics
Protein Function

Background:

Coronin proteins, including Dictyostelium discoideum Coronin7 (DdCRN7), are involved in cellular processes.
Human Coronin7 (CRN7) is implicated in membrane trafficking, and DdCRN7 shares high homology with it.

Purpose of the Study:

To elucidate the mechanism of DdCRN7 action, focusing on its relationship with the actin cytoskeleton.
To investigate the role of DdCRN7 in cellular functions like chemotaxis and phagocytosis.

Main Methods:

Studied actin-related aspects of DdCRN7 function.
Investigated DdCRN7 binding to F-actin in vitro and in vivo.
Analyzed DdCRN7 localization within the cytoskeleton and its sensitivity to actin-disrupting drugs.

Main Results:

DdCRN7 directly binds to F-actin, protecting actin filaments from depolymerization.
DdCRN7 associates with F-actin in vivo, localizing to the Triton X-100-insoluble cytoskeleton.
DdCRN7 distribution is sensitive to drugs that affect the actin cytoskeleton.

Conclusions:

DdCRN7 plays a crucial role in regulating the actin cytoskeleton.
The interaction of DdCRN7 with F-actin underlies its involvement in chemotaxis and phagocytosis.